Protein dynamics and function from solution state NMR spectroscopy

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KOVERMANN, Michael, Per ROGNE, Magnus WOLF-WATZ, 2016. Protein dynamics and function from solution state NMR spectroscopy. In: Quarterly Reviews of Biophysics. 49, e6. ISSN 0033-5835. eISSN 1469-8994

@article{Kovermann2016Prote-33978, title={Protein dynamics and function from solution state NMR spectroscopy}, year={2016}, doi={10.1017/S0033583516000019}, volume={49}, issn={0033-5835}, journal={Quarterly Reviews of Biophysics}, author={Kovermann, Michael and Rogne, Per and Wolf-Watz, Magnus}, note={Article Number: e6} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/33978"> <dcterms:title>Protein dynamics and function from solution state NMR spectroscopy</dcterms:title> <dc:contributor>Kovermann, Michael</dc:contributor> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/33978"/> <dcterms:rights rdf:resource="http://nbn-resolving.de/urn:nbn:de:bsz:352-20150914100631302-4485392-8"/> <dc:creator>Rogne, Per</dc:creator> <dcterms:abstract xml:lang="eng">It is well-established that dynamics are central to protein function; their importance is implicitly acknowledged in the principles of the Monod, Wyman and Changeux model of binding cooperativity, which was originally proposed in 1965. Nowadays the concept of protein dynamics is formulated in terms of the energy landscape theory, which can be used to understand protein folding and conformational changes in proteins. Because protein dynamics are so important, a key to understanding protein function at the molecular level is to design experiments that allow their quantitative analysis. Nuclear magnetic resonance (NMR) spectroscopy is uniquely suited for this purpose because major advances in theory, hardware, and experimental methods have made it possible to characterize protein dynamics at an unprecedented level of detail. Unique features of NMR include the ability to quantify dynamics (i) under equilibrium conditions without external perturbations, (ii) using many probes simultaneously, and (iii) over large time intervals. Here we review NMR techniques for quantifying protein dynamics on fast (ps-ns), slow (μs-ms), and very slow (s-min) time scales. These techniques are discussed with reference to some major discoveries in protein science that have been made possible by NMR spectroscopy.</dcterms:abstract> <dcterms:issued>2016</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-05-18T09:07:08Z</dcterms:available> <dc:contributor>Wolf-Watz, Magnus</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-05-18T09:07:08Z</dc:date> <dc:creator>Wolf-Watz, Magnus</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Rogne, Per</dc:contributor> <dc:creator>Kovermann, Michael</dc:creator> </rdf:Description> </rdf:RDF>

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